Annotation inferences using phylogenetic trees
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification.
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Immunopurification plus mass spectrometry of the human NADH dehydrogenase identified 42 subunit polypeptides, establishing NDUFB10 as a genuine component of Complex I.
"we can resolve and identify the human homologues of 42 polypeptides"
AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins.
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NDUFB10 is a nuclear-encoded mitochondrial preprotein lacking a cleavable presequence that binds the import receptors Tom20 and Tom22 in vitro (used as a control substrate in this AIP study).
"other mitochondrial preproteins, ATP/ADP carrier protein and NDUFB10, which lack a cleavable presequence, also bound to AIP as well as to Tom20"
Huntingtin interacting proteins are genetic modifiers of neurodegeneration.
A proteome-scale map of the human interactome network.
Accessory subunits are integral for assembly and function of human mitochondrial complex I.
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Human Complex I has 14 conserved core subunits essential for enzymatic function plus 31 accessory subunits (including NDUFB10) whose loss destabilizes co-module subunits and impairs assembly of a functional complex.
"Bacterial and human complex I share 14 core subunits that are essential for enzymatic function"
Mutations in the accessory subunit NDUFB10 result in isolated complex I deficiency and illustrate the critical role of intermembrane space import for complex I holoenzyme assembly.
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Biallelic NDUFB10 mutations cause isolated complex I deficiency (fatal infantile lactic acidosis, cardiomyopathy); NDUFB10 is a P_D-domain accessory subunit imported and oxidatively folded by CHCHD4/MIA40, and its loss perturbs holoenzyme assembly at the ~830 kDa stage.
"which encodes an accessory subunit located within the"
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NDUFB10 lies parallel to the membrane on the IMS face spanning ND4 and ND5 and, unlike most P_D accessory subunits, has no transmembrane domain.
"the bovine homolog PDSW of human NDUFB10 appears to be located parallel to the membrane on the IMS face spanning ND4 and ND5"
Architecture of Human Mitochondrial Respiratory Megacomplex I(2)III(2)IV(2).
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Cryo-EM of the human respiratory megacomplex resolved individual Complex I subunits, confirming NDUFB10 as a component located in the inner membrane.
"the precise assignment of individual subunits of human CI and CIII"
Assembly of mammalian oxidative phosphorylation complexes I-V and supercomplexes.
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Review of OXPHOS complex assembly; core proteins perform catalysis while supernumerary subunits play essential roles in assembly, regulation and stability.
"a large number of 'supernumerary' subunits that play essential roles in assembly, regulation and stability"
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
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NDUFB10 is detected in the high-confidence human mitochondrial proteome, confirming its mitochondrial localization.
"Quantitative high-confidence human mitochondrial proteome"
cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed.
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Characterized the cDNA of NDUFB10 as one of the nuclear-encoded Complex I subunits in the hydrophobic-protein fraction; the complex transports electrons from NADH to ubiquinone coupled to proton translocation.
"all located within the hydrophobic protein (HP) fraction of complex I"
Complex I oxidises NADH to NAD+, reduces CoQ to CoQH2
Intermediate 1 binds HP subcomplex to form Intermediate 2
Peripheral arm subunits bind the 815kDa complex to form a 980kDa complex
Intermediate 2 binds MT-ND1:NDUFAF5:NDUFAF6 to form a 315kDa subcomplex
The MCIA complex, NDUFAF2-7 all dissociate from the 980kDa complex, resulting in Complex I
ND4, ND5 bind the 550kDa complex to form the 815kDa complex
The 315kDa subcomplex binds the 370kDa subcomplex to form the 550kDa complex